1it1
From Proteopedia
(New page: 200px<br /><applet load="1it1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1it1" /> '''Solution structures of ferrocytochrome c3 fr...) |
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| - | [[Image:1it1.jpg|left|200px]]<br /><applet load="1it1" size=" | + | [[Image:1it1.jpg|left|200px]]<br /><applet load="1it1" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structures of ferrocytochrome c3 from Desulfovibrio vulgaris Miyazaki F'''<br /> | '''Solution structures of ferrocytochrome c3 from Desulfovibrio vulgaris Miyazaki F'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Heteronuclear NMR spectroscopy was performed to determine the solution | + | Heteronuclear NMR spectroscopy was performed to determine the solution structure of (15)N-labeled ferrocytochrome c(3) from Desulfovibrio vulgaris Miyazaki F (DvMF). Although the folding of the reduced cytochrome c(3) in solution was similar to that of the oxidized one in the crystal structure, the region involving hemes 1 and 2 was different. The redox-coupled conformational change is consistent with the reported solution structure of D. vulgaris Hildenborough ferrocytochrome c(3), but is different from those of other cytochromes c(3). The former is homologous with DvMF cytochrome c(3) in amino acid sequence. Small displacements of hemes 1 and 2 relative to hemes 3 and 4 were observed. This observation is consistent with the unusual behavior of the 2(1)CH(3) signal of heme 3 reported previously. As shown by the (15)N relaxation parameters of the backbone, a region between hemes 1 and 2 has more flexibility than the other regions. The results of this work strongly suggest that the cooperative reduction of hemes 1 and 2 is based on the conformational changes of the C-13 propionate of heme 1 and the aromatic ring of Tyr43, and the interaction between His34 and His 35 through covalent and coordination bonds. |
==About this Structure== | ==About this Structure== | ||
| - | 1IT1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IT1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IT1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tetraheme protein]] | [[Category: tetraheme protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:23 2008'' |
Revision as of 11:15, 21 February 2008
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Solution structures of ferrocytochrome c3 from Desulfovibrio vulgaris Miyazaki F
Overview
Heteronuclear NMR spectroscopy was performed to determine the solution structure of (15)N-labeled ferrocytochrome c(3) from Desulfovibrio vulgaris Miyazaki F (DvMF). Although the folding of the reduced cytochrome c(3) in solution was similar to that of the oxidized one in the crystal structure, the region involving hemes 1 and 2 was different. The redox-coupled conformational change is consistent with the reported solution structure of D. vulgaris Hildenborough ferrocytochrome c(3), but is different from those of other cytochromes c(3). The former is homologous with DvMF cytochrome c(3) in amino acid sequence. Small displacements of hemes 1 and 2 relative to hemes 3 and 4 were observed. This observation is consistent with the unusual behavior of the 2(1)CH(3) signal of heme 3 reported previously. As shown by the (15)N relaxation parameters of the backbone, a region between hemes 1 and 2 has more flexibility than the other regions. The results of this work strongly suggest that the cooperative reduction of hemes 1 and 2 is based on the conformational changes of the C-13 propionate of heme 1 and the aromatic ring of Tyr43, and the interaction between His34 and His 35 through covalent and coordination bonds.
About this Structure
1IT1 is a Single protein structure of sequence from Desulfovibrio vulgaris with as ligand. Full crystallographic information is available from OCA.
Reference
Redox-coupled conformational alternations in cytochrome c(3) from D. vulgaris Miyazaki F on the basis of its reduced solution structure., Harada E, Fukuoka Y, Ohmura T, Fukunishi A, Kawai G, Fujiwara T, Akutsu H, J Mol Biol. 2002 Jun 7;319(3):767-78. PMID:12054869
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